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- PDB-1mx8: Two homologous rat cellular retinol-binding proteins differ in lo... -
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Basic information
Entry | Database: PDB / ID: 1mx8 | ||||||
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Title | Two homologous rat cellular retinol-binding proteins differ in local structure and flexibility | ||||||
![]() | CELLULAR RETINOL-BINDING PROTEIN I, HOLO | ||||||
![]() | LIPID BINDING PROTEIN / beta-barrel / helix-turn-helix / vitamin A / Retonol binding / Transport | ||||||
Function / homology | ![]() regulation of granulocyte differentiation / response to benzoic acid / The canonical retinoid cycle in rods (twilight vision) / Retinoid metabolism and transport / all-trans-retinol binding / retinoic acid biosynthetic process / vitamin A metabolic process / retinal binding / response to vitamin A / retinol metabolic process ...regulation of granulocyte differentiation / response to benzoic acid / The canonical retinoid cycle in rods (twilight vision) / Retinoid metabolism and transport / all-trans-retinol binding / retinoic acid biosynthetic process / vitamin A metabolic process / retinal binding / response to vitamin A / retinol metabolic process / retinoic acid metabolic process / retinol binding / lipid homeostasis / fatty acid transport / response to retinoic acid / lipid droplet / fatty acid binding / cell body / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing | ||||||
Model type details | minimized average | ||||||
![]() | Lu, J. / Cistola, D.P. / Li, E. | ||||||
![]() | ![]() Title: Two homologous rat cellular retinol-binding proteins differ in local conformational flexibility. Authors: Lu, J. / Cistola, D.P. / Li, E. #1: ![]() Title: Binding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics Authors: Lu, J. / Lin, C.L. / Tang, C. / Ponder, J.W. / Kao, J.L. / Cistola, D.P. / Li, E. #2: ![]() Title: The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: comparison with the X-ray structure Authors: Lu, J. / Lin, C.L. / Tang, C. / Ponder, J.W. / Kao, J.L.F. / Cistola, D.P. / Li, E. #3: ![]() Title: Crystallographic studies on a family of cellular lipophilic transport proteins. Refinement of P2 myelin protein and the structure determination and refinement of cellular retinol-binding ...Title: Crystallographic studies on a family of cellular lipophilic transport proteins. Refinement of P2 myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans-retinol Authors: Cowan, S.W. / Newcomer, M.E. / Jones, T.A. #4: ![]() Title: Crystal structures of holo and apo-cellular retinol-binding protein II Authors: Winter, N.S. / Bratt, J.M. / Banaszak, L.J. #5: ![]() Title: Structure and backbone dynamics of apo- and holo-cellular retinal-binding protein in solution Authors: Franzoni, L. / Lucke, C. / Perez, C. / Cavazzini, D. / Rademacher, M. / Ludwig, C. / Spisni, A. / Rossi, G.L. / Ruterjans, H. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
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PDB format | ![]() | 906.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 15724.871 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-RTL / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: Triple resonance experiments for the 1H, 15N and 13C resonance assignments included the following: HNCO CBCACONNH HNCACB CBCACOCAHA HCCH-TOCSY 15N-resolved TOCSY-HSQC; The intra-ligand NOE ...Text: Triple resonance experiments for the 1H, 15N and 13C resonance assignments included the following: HNCO CBCACONNH HNCACB CBCACOCAHA HCCH-TOCSY 15N-resolved TOCSY-HSQC; The intra-ligand NOE constraints as well as ligand-protein NOE constraints were obtained from 2D 13C and 15N double half-filtered experiment |
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Sample preparation
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||||||||||||
NMR spectrometer |
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Processing
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Refinement | Method: distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 50 / Conformers submitted total number: 25 |